Supplier: Stemcell Technologies

Monocyte chemotactic protein-1 (MCP-1), also known as CCL2, is a member of the CC family of chemokines. The protein is primarily induced by platelet-derived growth factor (PDGF) gene (Cochran et al.). The biological effects of MCP-1 are mediated via the specific G-protein-coupled receptor CCR2 which in turn activates signal transduction pathways leading to monocyte transmigration (Sozzani et al.). Migration of monocytes from the bloodstream across the vascular endothelium is required for routine immunological surveillance of tissues, as well as other immunomodulatory effects. MCP-1 is produced by a variety of cell types, including fibroblasts and endothelial, epithelial, smooth muscle, mesangial, astrocytic, monocytic, and microglial cells, which are important for antiviral responses in the peripheral circulations and in tissues (Cushing et al.; Deshmane et al.). MCP-1 plays a role in physiological processes such as neurogenesis, neuroprotection, and neurotransmission and has important implications in neurological disorders such as multiple sclerosis and Alzheimer’s disease, in which it is produced during neuroinflammation at the sites of lesions (Conductier et al.).

Supplier: Adipogen

Human hepatocyte growth factor (HGF) is synthesized as a biologically inactive single chain precursor, which is cleaved by a specific, extracellular serum serine protease to a fully active heterodimer. It stimulates the motility and invasion of several cancer cell types and can induce angiogenesis. All biological responses induced by HGF are elicited by binding to its transmembrane tyrosine kinase receptor. HGF function is essential for normal development. Knockout studies have demonstrated that both ligand and receptor deficient mice display an embryonic lethal phenotype. HGF synergizes with basic FGF in the induction of angiogenesis. HGF is a potent mitogen for mature parenchymal hepatocyte cells and is a pleiotrophic cytokine. It acts as growth factor for a broad spectrum of tissues and cell types. It has no detectable protease activity. It is an activating ligand for the receptor tyrosine kinase MET by binding and promoting its dimerization.

Supplier: Stemcell Technologies

Interleukin 1 beta (IL-1β) is synthesized as an inactive precursor protein or pro-IL-1β. This precursor is cleaved intracellularly by caspase 1 (IL-1β convertase) to form the active form of the protein that is later secreted (Allan et al.). IL-1β binds to IL-1 receptor and activates intracellular signaling via the MAPK or NF-kB pathway. IL-1β is released by monocytes, tissue macrophages, and dendritic cells in response to infection or injury and induces expression of acute-phase proteins. It also promotes the infiltration of inflammatory and immunocompetent cells from the circulation into the extravascular space and affected tissues, by stimulating the expression of adhesion molecules on endothelial cells. IL-1β also affects other immune cells; for example, it co-stimulates T cell functions together with antigen or mitogen. It also stimulates Th17 differentiation and B cell proliferation in an IL-6-dependent manner. Mice deficient in IL-1β do not show phenotypical differences from wild-type mice; however, they have a reduced response to inflammation, suggesting that IL-1β plays a key role in inflammatory diseases (Dinarello).

Supplier: Adipogen

The TIM (T cell/transmembrane, immunoglobulin and mucin) family plays a critical role in regulating immune responses, including allergy, asthma, transplant tolerance, autoimmunity and the response to viral infections. The unique structure of TIM immunoglobulin variable region domains allows highly specific recognition of phosphatidylserine (PtdSer), exposed on the surface of apoptotic cells. Tim-3, a type I transmembrane protein, contains an immunoglobulin and a mucin-like domain in its extracellular portion and a tyrosine phosphorylation motif in its cytoplasmic portion. TIM-3 is preferentially expressed on Th1 and Tc1 cells, and generates an inhibitory signal resulting in apoptosis of Th1 and Tc1 cells. TIM-3 is also expressed on some dendritic cells and can mediate phagocytosis of apoptotic cells and cross-presentation of antigen. Tim-3 functions to inhibit aggressive Th1-mediated auto- and alloimmune responses. Tim-3 pathway blockade by administration of Tim-3:Fc fusion protein accelerates diabetes in nonobese diabetic mice, causes hyperproliferation of Th1 cells and Th1 cytokine release in an experimental autoimmune encephalomyelitis (EAE) model and prevents acquisition of transplantation tolerance induced by costimulation blockade.

Supplier: Anaspec

Matrix metalloproteinases (MMPs) belong to a family of secreted or membrane-associated zinc endopeptidases capable of digesting extracellular matrix components. MMP-12 (macrophage elastase) is involved in smoke-induced emphysema, tumor and other diseases. MMP-12 is secreted as a 54-kDa zymogen and becomes the mature 45-kDa active form after proteolytic cleavage. MMP-12 has a broad range of substrates, including α-1 proteinase inhibitor, α-2 antiplasmin, plasminogen activator inhibitor-2, collagen IV, laminin, fibronectin, elastin, but not interstitial collagens.

The sequence (Accession # NP_002417) corresponding to the catalytic domain (aa 106-267) of Human MMP-12 was expressed in E. coli. The recombinant human MMP-12 was purified from bacterial lysate and refolded using proprietary technique. The molecular weight of the recombinant Human MMP-12 Catalytic Domain is 18 kDa.

Supplier: Anaspec

Matrix metalloproteinases (MMP’s) belong to a family of secreted or membrane-associated zinc endopeptidases capable of digesting extracellular matrix components. MMP-1 (collagenase-1) is involved in tumor development and metastasis and rheumatoid arthritis. It is proposed as a therapeutic target for these diseases. Native pro-MMP-1 is prepared from culture medium of human rheumatoid synovial fibroblasts. MMP-1 is secreted as pro-enzyme, which consists of a propeptide of 80 amino acids, a catalytic domain of 162 amino acids, a 16-residue linker region, and a hemopexin domain of 189 amino acids. The native pro-MMP-1 has a major Mr 52-kDa unglycosylated and a minor Mr 57-kDa glycosylated form. The proteolytic activation of the 57/52-kDa species will form 47/42-kDa active collagenase, and a 22-kDa C-terminal fragment
The apparent Mr on SDS-PAGE is approximately 56kDa/52 kDa. The pro-MMP-1 can be fully activated by incubating with 1 mM APMA at 37°C for 3 hr. Its activity can be measured by FRET peptides. 10-20 ng of enzyme is sufficient for FRET-based assay

Supplier: Stemcell Technologies

Interleukin 33 (IL-33) is a pro-inflammatory cytokine from the IL-1 family. It binds to the ST2 receptor and activates NF-kB and MAPK pathways. IL-33 is expressed by epithelial cells, smooth muscle cells, and fibroblasts in various tissues and organs, as well as resting basophils, mast cells, eosinophils, natural helper cells, group 2 innate lymphoid cells, dendritic cells, and activated macrophages (Schmitz et al.; Yasuda et al.). It contributes to allergic inflammation by stimulating production of the cytokines IL-4, IL-5, and IL-13 in Th2 cells, and stimulates host defense against microbial and viral infections (Liew; Yasuda et al.). In the central nervous system, IL-33 is produced by endothelial cells and astrocytes. It induces proliferation of microglia and mediates production of pro-inflammatory cytokines (Yasuoka et al.).

Supplier: Stemcell Technologies

Nerve growth factor (NGF)-beta is a prototypical member of the neurotrophin family and has a role in the survival and growth of neural cells, regulating cell growth, promoting differentiation into neurons, and neuron migration. The beta subtype of NGF is biologically active in comparison to the alpha-2 and gamma-2 subtypes. NGF-beta in its secreted form can bind to tyrosine kinase A (trkA) receptor with high affinity and to p75 (NTR) with low affinity (Levi and Alemà; Sofroniew et al.). NGF has been shown to possess pro-inflammatory and pro-fibrogenic properties (Micera et al.). It has also been shown that overexpression of NGF-beta promotes differentiation of bone marrow mesenchymal stem cells into neurons through regulation of AKT and MAPK pathways (Yuan et al.). This product is animal component-free.

Supplier: Stemcell Technologies

Interleukin 9 (IL-9) has pleiotropic functions in the immune system and signals through its specific IL-9 receptor (IL-9R) (Renauld et al.). IL-9/IL-9R signaling pathway mainly targets the downstream activation of JAK/STAT (janus kinase/signal transducer and activator of transcription) and subsequent phosphorylation cascades initiated by multiple kinases including IRS–PI3K–PKB (insulin receptor substrate, phosphatidyl-inositol 3-kinases, protein kinase-B) and ERK (Knoops and Renauld; Fontaine et al.). IL-9 has been shown to have a role in Th1/Th17-mediated inflammation and in regulatory T cell responses (Singh et al.; Goswami and Kaplan). IL-9/IL-9R signaling pathway represents a novel endogenous anti-apoptotic mechanism for cortical neurons (Fontaine et al.). IL-9 secreting T cells, termed Th9 cells, contribute to both effective immunity and immunopathological disease, and have been shown to have a role in the treatment of allergic and autoimmune disease (Kaplan et al.).

Supplier: Stemcell Technologies

Basic fibroblast growth factor (bFGF) is a prototypic member of the fibroblast growth factor family. Cytokines in the FGF family possess broad mitogenic and cell survival activities (Folkman and Klagsbrun; Kimelman and Kirschner) and are involved in a variety of biological processes including cell proliferation, differentiation, survival, and apoptosis (Folkman and Klagsbrun; Klagsbrun; Rifkin and Moscatelli). bFGF has the β-trefoil structure (Ponting and Russell), binds to the four FGF receptor (FGFR) family members, and activates JAK/STAT, PI3K, ERK1/2, and other receptor tyrosine kinase (RTK) signaling pathways. It supports the maintenance of undifferentiated human embryonic stem cells (Xu et al.; Kang et al.), stimulates human embryonic stem cells to form neural rosettes (Zhang et al.), and improves proliferation of human mesenchymal stem cells and enhances chondrogenic differentiation (Solchaga et al.).

Supplier: Stemcell Technologies

Flt3/Flk-2 (Fms-like tyrosine kinase 3/fetal liver kinase-2) Ligand is a hematopoietic cytokine that plays an important role as a co-stimulatory factor in the proliferation, differentiation, and survival of hematopoietic stem and progenitor cells and in the development of the immune system (Hannum et al.). Flt3/Flk-2 Ligand, together with stem cell factor and thrombopoietin, is commonly used to promote expansion of primitive CD34+ hematopoietic cells in culture. In combination with myeloid cytokines such as GM-CSF, G-CSF, or M-CSF, Flt3/Flk-2 Ligand enhances the growth and numbers of clonogenic myeloid progenitor cells. In synergy with the interleukins IL-3, IL-4, IL-7, IL-11, IL-12, IL-15, and GM-CSF and TNF-α, Flt3/Flk-2 Ligand regulates the development of various lymphoid progenitor cells, including dendritic cell, B cell, T cell, and NK cell progenitors. In contrast, Flt3/Flk-2 Ligand has no significant effect on erythropoiesis or megakaryopoiesis (Drexler andamp; Quentmeier; Wodnar-Filipowicz). Flt3/Flk-2 Ligand exists as membrane-bound and soluble isoforms. Both isoforms are biologically active and signal through the class III tyrosine kinase receptor (Flt3/Flk-2, CD135; Rosnet et al.). Flt3/Flk-2 Ligand is produced by a variety of cell types, including uncommitted and committed hematopoietic cells and stromal fibroblasts, whereas expression of the Flt3/Flk-2 receptor is restricted to CD34+ hematopoietic stem and progenitor cells. Flt3/Flk-2 receptor is also expressed on leukemic cells and outside the hematopoietic system in the brain, placenta, and testis (Drexler andamp; Quentmeier; Hannum et al.).

Supplier: Stemcell Technologies

Oncostatin M (OSM) is a member of interleukin 6 (IL-6) family of cytokines and bears close resemblance to leukemia inhibitory factor (LIF) and granulocyte colony-stimulating factor (G-CSF) in amino acid sequence and its modulation of differentiation in a variety of cell types (Rose and Bruce). OSM signals through type I receptor (consisting of gp130 and LIF receptor [LIFR]) and type II receptor (consisting of gp130 and OSM receptor [OSMR]), which eventually activate the JAK/STAT pathway (Auguste et al.; Gómez-Lechón). OSM is primarily produced by activated T cells and monocytes, and also by activated macrophages, neutrophils, mast cells, and dendritic cells. OSM is also produced within the bone microenvironment by cells of both hematopoietic and mesenchymal origin, including osteocytes and osteoblasts. OSM is involved in differentiation, cell proliferation, hematopoiesis, and inflammation, and also has been shown to have implications in liver development and bone formation and resorption (Sims and Quinn; Tanaka and Miyajima). This product is animal component-free.

Supplier: Stemcell Technologies

Platelet-derived growth factor (PDGF) is a dimeric glycoprotein consisting of two disulfide bridge-stabilized polypeptide chains, A and B, which are assembled as heterodimers (PDGF-AB) or homodimers (PDGF-AA and PDGF-BB) (Fretto et al.; Westermark and Heldin). PDGF signals through the receptor tyrosine kinases PDGFRalpha and PDGFRbeta. PDGF-induced migration has been shown to involve MEK/ERK, EGFR, Src, and PI3K/Akt signaling pathways (Kim et al.). PDGF is a potent mitogen for cells of mesenchymal origin- like fibroblasts, glial cells, and vascular smooth muscle cells. PDGF has been implicated in pathogenesis of atherosclerosis, glomerulonephritis, cancer, and in the contraction of vascular smooth muscle cells of rat aortic tissues (Fretto et al.; Sachinidis et al.). PDGF-BB is secreted by osteoblasts to induce mesenchymal stem cell migration and angiogenesis. It has also been shown that PDGF-BB is secreted by preosteoclasts during bone modeling and remodeling to induce angiogenesis and thus proper osteogenesis (Xie et al.). This product is animal component-free.

Supplier: Stemcell Technologies

Interleukin 21 (IL-21) is a pleiotropic cytokine that is composed of four α-helical bundles and primarily produced by natural killer T (NKT) cells, T follicular helper (Tfh) cells, and Th17 cells (Spolski and Leonard 2008). IL-21 signals via heterodimers of the IL-21 receptor (IL-21R) and the IL2RG encoded common cytokine receptor γ-chain (Parrish-Novak et al.; Ozaki K et al. 2000), and utilizes the JAK/STAT, MAPK, and PI3K pathways (Spolski and Leonard 2014). IL-21 has been shown to have a critical role in regulating immunoglobulin production and differentiation of the pro-inflammatory Th17 population of cells (Ozaki et al. 2002; Nurieva et al.). Additionally, IL-21 specifically sustains CD8+ T cell effector activity and provides a mechanism of CD4+ T cell help during chronic viral infection (Elsaesser et al.). IL-21 signaling was also found critical for the development of type 1 diabetes in NOD mice (Sutherland et al.) and control of T cell autoimmunity by regulatory B cells (Yoshizaki et al.).

Supplier: Adipogen

Interleukin-27 (IL-27) is a heterodimeric group 2 receptor ligand molecule that belongs to the IL-6/IL-12 family of long type I cytokines. It is composed of EBI3 (EBV-induced gene 3), a 34 kDa glycoprotein that is related to the p40 subunit of IL-12 and IL-23, and p28, the cloned 28 kDa glycoprotein that is related to the p35 chain of IL-12. IL-27 is expressed by monocytes, endothelial cells and dendritic cells. IL-27 binds to and signals through a heterodimeric receptor complex composed of WSX1 (TCCR) and gp130. Evidence suggests IL-27 interacts only with WSX-1. IL-27 has both anti- and proinflammatory properties. As an antiinflammatory, IL-27 seems to induce a general negative feedback program that limits T and NK-T cell activity. At the onset of infection, IL-27 induces an IL-12 receptor on naïe CD4+ T cells, making them susceptible to subsequent IL-12 activity (and possible Th1 development). Notably, IL-12 family cytokines are both induced and inhibited by bacterial products. Microbes promote IL-27 secretion through TLR4, and also block IL-27 production via C5a induction.

Supplier: Adipogen

Interleukin-33 (IL-33; HF-NEV; IL-1F11), a member of the IL-1 family of cytokines, is expressed by many cell types following pro-inflammatory stimulation and is thought to be released upon cell lysis. IL-33 binds to and signals through ST2 (IL-1R1) and its stimulation recruits MYD88, IRAK, IRAK4 and TRAF6, followed by phosphorylation of ERK1 (MAPK3) / ERK2 (MAPK1), p38 (MAPK14) and JNK. The ability of IL-33 to target numerous immune cell types, like Th2-like cells, mast cells and B1 cells, and to induce cytokine and chemokine production underlines its potential in influencing the outcome of a wide range of diseases, such as arthritis, asthma, atopic allergy & anaphylaxis, cardiovascular disease/atherosclerosis, nervous system diseases and sepsis. IL-33 facilitates Treg expansion in vitro and in vivo. Recently, IL-33 has been involved in adipocyte differentiation. The biological activity of IL-33 at its receptor ST2 is rapidly terminated in the extracellular environment by its oxidation (formation of two disulfide bridges), resulting in an extensive conformational change that disrupts the ST2 binding site. Mutations at amino acids C208S/C232S protect IL-33 from oxidation and increase its activity.

Supplier: Adipogen

Recombinant human soluble vascular endothelial growth factor receptor-1 (sVEGFR-1) is the naturally occurring form and is a glycosylated monomeric protein. The biological function of sVEGFR-1 seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. VEGFR-1 is a tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFB and PGF, and plays an essential role in the development of embryonic vasculature, the regulation of angiogenesis, cell survival, cell migration, macrophage function, chemotaxis and cancer cell invasion. It may play an essential role as a negative regulator of embryonic angiogenesis by inhibiting excessive proliferation of endothelial cells. It can promote endothelial cell proliferation, survival and angiogenesis in adulthood. Its function in promoting cell proliferation seems to be cell-type specific. Promotes PGF-mediated proliferation of endothelial cells, proliferation of some types of cancer cells, but does not promote proliferation of normal fibroblasts (in vitro). It has a very high affinity for VEGFA and relatively low protein kinase activity. It may function as a negative regulator of VEGFA signaling by limiting the amount of free VEGFA and preventing its binding to KDR. Modulates KDR signaling by forming heterodimers with KDR. Ligand binding leads to the activation of several signaling cascades. Activation of phospholipase C-gamma (PLCG) leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leading to activation of phosphatidylinositol kinase and the downstream signaling pathway. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Phosphorylates SRC and YES1 and may also phosphorylate CBL.

Supplier: Adipogen

NF-kappaB is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappaB is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The heterodimeric p65-p50 complex is the most abundant complex. The dimers bind at kappaB sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappaB sites that they can bind with distinguishable affinity and specificity.Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappaB complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappaB inhibitor (I-kappaB) family. In a conventional activation pathway, I-kappaB is phosphorylated by I-kappaB kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappaB complex which translocates to the nucleus. NF-kappaB heterodimeric p65-p50 and p65-c-Rel complexes are transcriptional activators. The NF-kappaB p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappaB complex.

Supplier: Stemcell Technologies

Ciliary neurotrophic factor (CNTF) is a neurotrophic factor that belongs to the four-helix bundle cytokine family and is structurally related to interleukin 6 (IL-6), interleukin 11 (IL-11), leukemia inhibitory factor (LIF), and oncostatin M (OSM). CNTF binds to its receptor CNFTRα and induces formation of a heterodimer of the signal transducing IL-6 receptor gp130 and LIF receptor (LIFR)-β, which triggers JAK/STAT, ERK, and PI3K signaling cascades (Schuster et al.). CNTF plays an important role in neurogenesis and the differentiation of neural stem cells and has been suggested to possess a therapeutic role in treating neurological disorders (Ding et al.; Oppenheim et al.). CNTF has also been shown to protect rod photoreceptors from light-induced damage and have therapeutic effects on retinal degenerative diseases caused by genetic defect or damage induced by toxins, autoantibodies, or strong light (Pernet et al.; Rhee et al.). Another therapeutic role of CNTF has been reported in protecting oligodendrocytes from death induced by apoptosis (Louis et al.). Additionally, CNTF is commonly used to differentiate human pluripotent stem cell (hPSC)-derived neural progenitor cells into astrocytes (Krencik and Zhang). This product is animal component-free.

Supplier: Stemcell Technologies

Interleukin 11 (IL-11) is a pleiotropic cytokine with effects on various tissues including the bone marrow, brain, and intestinal mucosa (Du andamp; Williams). It belongs to the IL-6 family of cytokines that share a common signal transducer, gp130. IL-11 induces the proliferation of hematopoietic stem cells (Lemoli et al.) and megakaryocytic progenitor cells (Bruno et al.), the maturation of megakaryocytes (Burstein et al.), and the production of platelets (Neben et al.). IL-11 is produced by a variety of cell types including hematopoietic cells, mesenchymal cells, epithelial cells, and neuronal cells. It was first cloned from a cDNA library of the human bone marrow-derived stromal cell line KM-102 (Kawashima et al.). The binding of IL-11 to its receptor induces heterodimerization with the gp130 subunit and activation of JAK tyrosine kinases. IL-11 was the first pharmacologic agent approved for the treatment of chemotherapy-induced thrombocytopenia. IL-11 also plays a role in cancer progression by inducing the proliferation of epithelial cancer cells and the survival of metastatic cells at distant organs. Recently, IL-11 has gained interest for its role in the pathogenesis of diseases in dysregulated mucosal homeostasis associated with STAT3 upregulation, including gastrointestinal cancers (Putoczki et al.).

Supplier: Stemcell Technologies

Granulocyte-macrophage colony-stimulating factor (GM-CSF) promotes the proliferation and differentiation of hematopoietic progenitor cells and the generation of neutrophils, eosinophils, and macrophages. In synergy with other cytokines such as stem cell factor, IL-3, erythropoietin, and thrombopoietin, it also stimulates erythroid and megakaryocyte progenitor cells (Barreda et al.). GM-CSF is produced by multiple cell types, including stromal cells, Paneth cells, macrophages, dendritic cells (DCs), endothelial cells, smooth muscle cells, fibroblasts, chondrocytes, and Th1 and Th17 T cells (Francisco-Cruz et al.). The receptor for GM-CSF (GM-CSFR) is composed of two subunits: the cytokine-specific α subunit (GMRα; CD116) and the common subunit βc (CD131) shared with IL-3 and IL-5 receptors (Broughton et al.). GM-CSFR is expressed on hematopoietic cells, including progenitor cells and immune cells, as well as non-hematopoietic cells. Recombinant human GM-CSF (rhGM-CSF) promotes the production of myeloid cells of the granulocytic (neutrophils, eosinophils and basophils) and monocytic lineages in vivo. It has been tested for mobilization of hematopoietic progenitor cells and for treating chemotherapy-induced neutropenia in patients. GM-CSF is able to stimulate the development of DCs that ingest, process, and present antigens to the immune system (Francisco-Cruz et al.).

Supplier: Stemcell Technologies

Brain-derived neurotrophic factor (BDNF), like nerve growth factor (NGF), neurotrophin-3 (NT-3), and neurotrophin-4 (NT-4), is a member of the NGF family of neurotrophins, which are required for the differentiation and survival of specific neuronal subpopulations in both the central and the peripheral nervous systems (Minichiello and Klein; Minichiello et al.). BDNF binds with high affinity to the TRKB kinase receptor, and activates AKT and ERK pathways (Mattson et al.). It is expressed in hippocampus, cortex, and synapses of the basal forebrain. BDNF acts as a survival factor for human embryonic stem cells when plated on either feeder cells or Corning® Matrigel® (Pyle et al.). BDNF regulates synaptic transmission and plasticity at adult synapses in the central nervous system, contributes to adaptive neuronal responses including long-term potentiation, long-term depression, certain forms of short-term synaptic plasticity, as well as homeostatic regulation of neuronal excitability (Reichardt). It also has a role in neurogenesis by promoting survival and growth of dorsal root ganglion cells, and hippocampal and cortical neurons (Binder and Scharfman). BDNF, together with glial cell-derived neurotrophic factor (GDNF) and other supplements, is commonly used to differentiate human pluripotent stem cell (hPSC)-derived neural progenitor cells into neurons (Brafman). This product is animal component-free.

Supplier: Stemcell Technologies

Granulocyte colony-stimulating factor (G-CSF) is a member of the CSF family of glycoproteins that regulate hematopoietic cell proliferation, differentiation, and function. It is a key cytokine involved in the production of neutrophils and the stimulation of granulocyte colony formation from hematopoietic progenitor cells (Metcalf and Nicola). G-CSF causes a range of effects including a transient reduction of SDF-1 expression (Petit et al.), the activation of metalloproteases that cleave VCAM-1 (Levesque et al.), and the release of norepinephrine from the sympathetic nervous system (Katayama et al.), leading to the release or mobilization of hematopoietic stem cells from the bone marrow into the periphery. The G-CSF receptor is expressed on a variety of hematopoietic cells, including myeloid-committed progenitor cells, neutrophils, granulocytes, and monocytes. In addition to hematopoietic cells, G-CSF is also expressed in cardiomyocytes, neuronal cells, mesothelial cells, and endothelial cells. Mouse G-CSF was first purified from cultures of the WEHI-3B myelomonocytic leukemia cell line as the inducer of the terminal differentiation of WEHI-3B and other myeloid leukemia cell lines (Nicola et al.). It was later cloned in monkey COS cells from a cDNA library prepared with mRNA derived from mouse fibrosarcoma NFSA cells that produce G-CSF constitutively (Tsuchiya et al.). Binding of G-CSF to its receptor leads to activation of the JAK/STAT, MAPK, PI3K, and AKT signal transduction pathways.

Supplier: Abnova

Human DPYSL2 full-length ORF recombinant protein with GST-tag at N-terminal.

Supplier: New England Biolabs (NEB)

NEBExpress GamS nuclease inhibitor is a recombinant protein that inhibits Exonuclease V (RecBCD) activity and stabilizes linear DNA templates in E. coli based in vitro protein synthesis reactions.